Functional profiling of adenylation domains in nonribosomal peptide synthetases by competitive activity-based protein profiling

  • Chem Commun (Camb). 2015 Nov 11;51(87):15764-7. doi: 10.1039/c5cc04953a.
Shota Kasai  1 ,  Sho Konno  1 ,  Fumihiro Ishikawa  1 ,  Hideaki Kakeya  1
Affiliations
  • 1. Department of System Chemotherapy and Molecular Sciences, Division of Bioinformatics and Chemical Genomics, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo, Kyoto 606-8501, Japan. [email protected] [email protected].
PMID: 26365322 DOI: 10.1039/c5cc04953a
Abstract

We describe competitive activity-based protein profiling (ABPP) to accelerate the functional prediction and assessment of adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) in proteomic environments. Using a library of sulfamoyloxy-linked aminoacyl-AMP analogs, the competitive ABPP technique offers a simple and rapid assay system for adenylating Enzymes and provides insight into enzyme substrate candidates and enzyme active-site architecture.

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